CHST7

From Wikipedia, the free encyclopedia

Carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 7

Identifiers

CHST7; C6ST-2

External IDs

OMIM: 300375 MGI: 1891767 HomoloGene: 10531

Gene ontology
Molecular Function:	• N-acetylglucosamine 6-O-sulfotransferase activity • chondroitin 6-sulfotransferase activity • transferase activity
Cellular Component:	• membrane • integral to membrane • intrinsic to Golgi membrane
Biological Process:	• polysaccharide metabolic process • N-acetylglucosamine metabolic process • sulfur metabolic process • chondroitin sulfate biosynthetic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_019886 (mRNA)
NP_063939 (protein)

NM_021715 (mRNA)
NP_068361 (protein)

Location

Chr X: 46.32 - 46.34 Mb

Chr X: 19.22 - 19.25 Mb

Pubmed search

[1]

[2]

Carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 7, also known as CHST7, is a human gene.^[1]

This gene belongs to the sulfotransferase gene family. Sulfotransferases generate sulfated glycosaminoglycan (GAG) moities during chondroitin sulfate biosynthesis. They create considerable structural diversity among chondroitin sulfates by transferring sulfate with remarkable specificity for the underlying oligosaccharide substrate. This gene product mainly transfers sulfate to N-acetylgalactosamine. The regulated expression of each member of this gene family may be an important determinant of sulfated GAGs expression and the associated function of chondroitin sulfates as regulators of many biologic processes. This gene is part of a gene cluster on chromosome Xp11.23.^[1]

[edit] References

^ ^a ^b Entrez Gene: CHST7 carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 7.

[edit] Further reading

Liu T, Qian WJ, Gritsenko MA, et al. (2006). "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.". J. Proteome Res. 4 (6): 2070-80. doi:10.1021/pr0502065. PMID 16335952.
Ross MT, Grafham DV, Coffey AJ, et al. (2005). "The DNA sequence of the human X chromosome.". Nature 434 (7031): 325-37. doi:10.1038/nature03440. PMID 15772651.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932.
Thiselton DL, McDowall J, Brandau O, et al. (2002). "An integrated, functionally annotated gene map of the DXS8026-ELK1 interval on human Xp11.3-Xp11.23: potential hotspot for neurogenetic disorders.". Genomics 79 (4): 560-72. doi:10.1006/geno.2002.6733. PMID 11944989.
Bhakta S, Bartes A, Bowman KG, et al. (2001). "Sulfation of N-acetylglucosamine by chondroitin 6-sulfotransferase 2 (GST-5).". J. Biol. Chem. 275 (51): 40226-34. doi:10.1074/jbc.M006414200. PMID 10956661.
Uchimura K, Fasakhany F, Kadomatsu K, et al. (2000). "Diversity of N-acetylglucosamine-6-O-sulfotransferases: molecular cloning of a novel enzyme with different distribution and specificities.". Biochem. Biophys. Res. Commun. 274 (2): 291-6. doi:10.1006/bbrc.2000.3141. PMID 10913333.
Kitagawa H, Fujita M, Ito N, Sugahara K (2000). "Molecular cloning and expression of a novel chondroitin 6-O-sulfotransferase.". J. Biol. Chem. 275 (28): 21075-80. doi:10.1074/jbc.M002101200. PMID 10781596.
Shilatifard A, Merkle RK, Helland DE, et al. (1993). "Complex-type N-linked oligosaccharides of gp120 from human immunodeficiency virus type 1 contain sulfated N-acetylglucosamine.". J. Virol. 67 (2): 943-52. PMID 8419650.
Bernstein HB, Compans RW (1992). "Sulfation of the human immunodeficiency virus envelope glycoprotein.". J. Virol. 66 (12): 6953-9. PMID 1433500.